Crystal structure of the long Rib domain of the LPXTG-anchored surface protein from Limosilactobacillus reuteri.

Yi Xue, Zhen Wu, Xue Kang

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In one paragraph

Article in Acta crystallographica. Section F, Structural biology communications, 2024. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.

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1citing papers in PubMed

–field-weighted citation impact

1 · What the graph read from it

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3 · Its place in the literature

Who cites it

1 citing paper in PubMed.

Crystal structure of the Rib domain of the cell-wall-anchored surface protein from Limosilactobacillus reuteri.Acta crystallographica. Section F, Structural biology communications · 2024
Article

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5 · Who and what money

Authors and funding

3 authors.

Yi XueInstitute of Drug Discovery Technology, Ningbo University, Ningbo, Zhejiang 315211, People's Republic of China.

Zhen WuCollege of Food Science and Engineering, Ningbo University, Ningbo, Zhejiang 315211, People's Republic of China.

Xue KangInstitute of Drug Discovery Technology, Ningbo University, Ningbo, Zhejiang 315211, People's Republic of China.ORCID 0000-0002-2011-5580

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

The Rib domain, which is often found as tandem-repeat structural modules in surface proteins of Gram-positive bacteria, plays important roles in mediating interactions of bacteria with their environments and hosts. A comprehensive structural analysis of various Rib domains is essential to fully understand their impact on the structure and functionality of these bacterial adhesins. To date, structural information has been limited for this expansive group of domains. In this study, the high-resolution crystal structure of the second member of the long Rib domain, a unique subclass within the Rib-domain family, derived from Limosilactobacillus reuteri is presented. The data not only demonstrate a highly conserved structure within the long Rib domain, but also highlight an evolutionary convergence in structural architecture with other modular domains found in cell-adhesion molecules.

Indexed as

Limosilactobacillus reuteriModels, MolecularProtein DomainsAdhesins, BacterialAmino Acid SequenceBacterial ProteinsCrystallography, X-RayRecombinant ProteinsAdhesins, BacterialBacterial ProteinsRecombinant Proteinsbacterial adhesinsLimosilactobacillus reuterilong Rib domainsLPXTG-anchored surface proteinsRib domainsX-ray crystallography

Identifiers

PMID38699970

DOI10.1107/S2053230X24003868

PMCPMC11134729

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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.